K. Flade et al., Osteocalcin-controlled dissolution-reprecipitation of calcium phosphate under biomimetic conditions, CHEM MATER, 13(10), 2001, pp. 3596-3602
We have examined the influence of osteocalcin, one of the 10 most abundant
proteins of the human body, on hydroxyapatite (HAP, Ca-10(PO4)(6)(OH)(2)) f
ormation. Different functions in biomineralization are attributed to the bo
ne-specific protein osteocalcin because of its Ca2+ binding including HAP b
inding properties and its capability to inhibit HAP precipitation. To study
nucleation and crystal growth, a model system with osteocalcin-controlled
dissolution-reprecipitation of brushite (DCPD, CaHPO4. 2H(2)O) to HAP has b
een investigated. After DCPD crystals were grown from aqueous solution, the
y were exposed to an osteocalcin-containing buffer solution of pH 7.4. Thin
apatite-like crystals with hexagonal symmetry grew on the (010) brushite p
lanes. The apatite (0001) planes were fully covered with osteocalcin molecu
les. Thus, osteocalcin has been found to regulate HAP formation in two diff
erent ways: (i) it accelerates nucleation, and (ii) it acts as a specific i
nhibitor of the apatite (0001) plane, supressing crystal growth perpendicul
ar to this plane. A stress-induced growth model was developed illustrating
HAP growth along the brushite -HAP interface considering compressions in th
e protein-covered HAP crystals.